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2IPS

Crystal structure of a ternary complex of bovine lactoperoxidase with thiocyanate and iodide at 3.1 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
AHIS109

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424
ChainResidueDetails
AASP108
AGLU258

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424
ChainResidueDetails
AASP110
ATHR184
APHE186
AASP188
ASER190

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424
ChainResidueDetails
AHIS351

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
AARG255

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248
ChainResidueDetails
ASER198

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P11678
ChainResidueDetails
ATYR365

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248
ChainResidueDetails
AASN95
AASN205
AASN241
AASN332

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PDB entries from 2024-03-27

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